Leucine Enkephalin Analogues Containing a Conformationally Restrained N-Terminal Amino Acid Residue

1984 ◽  
Vol 73 (4) ◽  
pp. 457-460 ◽  
Author(s):  
Trevor Deeks ◽  
Peter A. Crooks ◽  
Roger D. Waigh
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Terminal Amino Acid ◽  
Leucine Enkephalin ◽  
Enkephalin Analogues ◽  
Terminal Amino ◽  
Conformationally Restrained

scholarly journals Phosphorus (V) porphyrin diaxially substituted with Leu-enkephalin

2004 ◽  
Vol 2 (3) ◽  
pp. 446-455 ◽  
Author(s):  
Mariusz Gajewski ◽  
Leszek Czuchajowski
Keyword(s):  
Amino Acids ◽  
Photodynamic Therapy ◽  
Amino Acid ◽  
Biologically Active ◽  
Solution Phase ◽  
Terminal Amino Acid ◽  
Leucine Enkephalin ◽  
Potential Applications ◽  
Biologically Active Peptide ◽  
Terminal Amino

AbstractSynthesis of the first phosphorus (V) porphyrin-peptide conjugate was successfully accomplished. A biologically active peptide, leucine enkephalin, was constructed on the phosphorus atom of the 5,10,15,20-meso-tetraphenylporphinato dichlorophosphorus (V) chloride. The method involved solution phase peptide synthesis. The first C-terminal amino acid in the sequence of the peptide was axially attached to the porphyrin through a linker, 3-aminopropanol, and the remainder of leucine enkephalin was synthesized by subsequent additions of amino acids. Leucine enkephalin-P(V) porphyrin conjugate represents a new group of compounds, and its synthesis broadens potential applications of P(V) porphyrine, e.g. in photodynamic therapy.

Plasma Oxytocinase: The Synthesis and Biological Properties of the First Prodoct of the Degradation of Oxytocin by this Enzyme

1974 ◽  
Vol 52 (1) ◽  
pp. 60-66 ◽  
Author(s):  
B. M. Ferrier ◽  
J. M. Hendrie ◽  
L. A. Branda
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Pregnant Women ◽  
Amino Acid Residue ◽  
Biological Properties ◽  
Milk Ejection ◽  
Terminal Amino Acid ◽  
Molecular Features ◽  
Marked Inhibition ◽  
Terminal Amino

Oxytocin is hydrolytically cleaved in the presence of plasma oxytocinase to give an acyclic peptide, tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-(S-cysteine)-cysteinyl-prolyl-leucyl-glycinamide (1,2-acyclic oxytocin). The synthesis of this peptide is described. It is shown to be of very low potency in milk-ejection-like activity and uterotonic activity. It does not inhibit the expression of these activities by oxytocin, suggesting that it does not interfere with the hormone's binding to target tissues. The presence of 1,2-acyclic oxytocin slightly inhibits the rate of degradation of oxytocin by plasma from pregnant women, in contrast to the marked inhibition of the degradation of cystine di-β-naphthylamide. The Km for the degradation of oxytocin is 30 times smaller than that of the degradation of cystine di-β-naphthylamide, which is of the same order as the Ki for the inhibition of the degradation of cystine di-β-naphthylamide by 1,2-acyclic oxytocin. These results, together with information on the substrate specificity of plasma oxytocinase with respect to the N-terminal amino acid residue, suggest that there are molecular features of oxytocin other than its N-terminal residue that facilitate its interaction with plasma oxytocinase.

The degradation of glycoproteins with lithium borohydride: Isolation and analysis ofO-glycopeptides with reducedC-terminal amino acid residue

2000 ◽  
Vol 26 (1) ◽  
pp. 45-53
Author(s):  
N. P. Arbatsky ◽  
L. M. Likhosherstov ◽  
M. V. Serebryakova ◽  
O. S. Brusov ◽  
V. N. Shibaev ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Terminal Amino Acid ◽  
Lithium Borohydride ◽  
Terminal Amino

scholarly journals Significance of the C-terminal amino acid residue in mengovirus RNA-dependent RNA polymerase

Virology ◽  
2007 ◽  
Vol 365 (1) ◽  
pp. 79-91 ◽  
Author(s):  
Tatiana M. Dmitrieva ◽  
Andrei V. Alexeevski ◽  
Galina S. Shatskaya ◽  
Elena A. Tolskaya ◽  
Anatoly P. Gmyl ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rna Polymerase ◽  
Amino Acid Residue ◽  
Terminal Amino Acid ◽  
Rna Dependent Rna Polymerase ◽  
Terminal Amino
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